(Q46903405)

English

Characterization of ankyrin repeat-containing proteins as substrates of the asparaginyl hydroxylase factor inhibiting hypoxia-inducible transcription factor.

scientific article published in January 2007

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10 January 2020

Characterization of ankyrin repeat-containing proteins as substrates of the asparaginyl hydroxylase factor inhibiting hypoxia-inducible transcription factor (English)

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10 January 2020

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10 January 2020

Rachel J Hampton-Smith

2

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10 January 2020

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Sarah Linke

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10 January 2020

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1 January 2007

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10 January 2020

Methods in Enzymology

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10 January 2020

435

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10 January 2020

61-85

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10 January 2020

Cell-specific regulation of hypoxia-inducible factor (HIF)-1alpha and HIF-2alpha stabilization and transactivation in a graded oxygen environment

1 reference

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Structural studies on 2-oxoglutarate oxygenases and related double-stranded beta-helix fold proteins

1 reference

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7 January 2021

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Posttranslational hydroxylation of ankyrin repeats in IkappaB proteins by the hypoxia-inducible factor (HIF) asparaginyl hydroxylase, factor inhibiting HIF (FIH)

1 reference

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Structural basis for Hif-1 alpha /CBP recognition in the cellular hypoxic response

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Structure of factor-inhibiting hypoxia-inducible factor 1: An asparaginyl hydroxylase involved in the hypoxic response pathway

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Absence of post-translational aspartyl beta-hydroxylation of epidermal growth factor domains in mice leads to developmental defects and an increased incidence of intestinal neoplasia

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Studies on the activity of the hypoxia-inducible-factor hydroxylases using an oxygen consumption assay

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Structure of factor-inhibiting hypoxia-inducible factor (HIF) reveals mechanism of oxidative modification of HIF-1 alpha

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Hypoxia requires notch signaling to maintain the undifferentiated cell state

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FeII/alpha-ketoglutarate-dependent hydroxylases and related enzymes

1 reference

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7 January 2021

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Hypoxia-inducible factor (HIF) asparagine hydroxylase is identical to factor inhibiting HIF (FIH) and is related to the cupin structural family

1 reference

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7 January 2021

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Characterization of the human prolyl 4-hydroxylases that modify the hypoxia-inducible factor

1 reference

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Development of a bicistronic vector driven by the human polypeptide chain elongation factor 1alpha promoter for creation of stable mammalian cell lines that express very high levels of recombinant proteins

1 reference

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The length of peptide substrates has a marked effect on hydroxylation by the hypoxia-inducible factor prolyl 4-hydroxylases

1 reference

https://api.crossref.org/works/10.1016%2FS0076-6879%2807%2935004-0

7 January 2021

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Catalytic properties of the asparaginyl hydroxylase (FIH) in the oxygen sensing pathway are distinct from those of its prolyl 4-hydroxylases

1 reference

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Differential growth factor regulation of aspartyl-(asparaginyl)-beta-hydroxylase family genes in SH-Sy5y human neuroblastoma cells

1 reference

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7 January 2021

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Factor inhibiting hypoxia-inducible factor (FIH) and other asparaginyl hydroxylases

1 reference

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Disruption of dimerization and substrate phosphorylation inhibit factor inhibiting hypoxia-inducible factor (FIH) activity

1 reference

https://api.crossref.org/works/10.1016%2FS0076-6879%2807%2935004-0

7 January 2021

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Asparagine hydroxylation of the HIF transactivation domain a hypoxic switch

1 reference

https://api.crossref.org/works/10.1016%2FS0076-6879%2807%2935004-0

7 January 2021

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FIH-1 is an asparaginyl hydroxylase enzyme that regulates the transcriptional activity of hypoxia-inducible factor

1 reference

https://api.crossref.org/works/10.1016%2FS0076-6879%2807%2935004-0

7 January 2021

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Structure of human FIH-1 reveals a unique active site pocket and interaction sites for HIF-1 and von Hippel-Lindau

1 reference

https://api.crossref.org/works/10.1016%2FS0076-6879%2807%2935004-0

7 January 2021

based on heuristic

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Ankyrin repeat: a unique motif mediating protein-protein interactions.

1 reference

https://api.crossref.org/works/10.1016%2FS0076-6879%2807%2935004-0

7 January 2021

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Substrate requirements of the oxygen-sensing asparaginyl hydroxylase factor-inhibiting hypoxia-inducible factor

1 reference

https://api.crossref.org/works/10.1016%2FS0076-6879%2807%2935004-0

7 January 2021

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FIH-1: a novel protein that interacts with HIF-1alpha and VHL to mediate repression of HIF-1 transcriptional activity

1 reference

https://api.crossref.org/works/10.1016%2FS0076-6879%2807%2935004-0

7 January 2021

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A fluorescence-based assay for 2-oxoglutarate-dependent oxygenases

1 reference

https://api.crossref.org/works/10.1016%2FS0076-6879%2807%2935004-0

7 January 2021

based on heuristic

inferred from DOI database lookup

Hypoxia-inducible factor asparaginyl hydroxylase (FIH-1) catalyses hydroxylation at the beta-carbon of asparagine-803

1 reference

https://api.crossref.org/works/10.1016%2FS0076-6879%2807%2935004-0

7 January 2021

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Consensus-derived structural determinants of the ankyrin repeat motif

1 reference

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Structural requirements for assembly of the CSL.intracellular Notch1.Mastermind-like 1 transcriptional activation complex

1 reference

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Oxygen-dependent asparagine hydroxylation

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Kinetic dissection of the catalytic mechanism of taurine:alpha-ketoglutarate dioxygenase (TauD) from Escherichia coli

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Decarboxylation of alpha-ketoglutarate coupled to collagen proline hydroxylase

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Signalling hypoxia by HIF hydroxylases

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Targeting HIF-1 for cancer therapy

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Use of novel monoclonal antibodies to determine the expression and distribution of the hypoxia regulatory factors PHD-1, PHD-2, PHD-3 and FIH in normal and neoplastic human tissues.

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Calcium-binding EGF-like modules in coagulation proteinases: function of the calcium ion in module interactions

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Hydroxylation of aspartic acid in domains homologous to the epidermal growth factor precursor is catalyzed by a 2-oxoglutarate-dependent dioxygenase

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Genetic analysis of the role of the asparaginyl hydroxylase factor inhibiting hypoxia-inducible factor (FIH) in regulating hypoxia-inducible factor (HIF) transcriptional target genes [corrected].

1 reference

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Roles of jumonji and jumonji family genes in chromatin regulation and development

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Current perspectives on histone demethylases

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Methylation: lost in hydroxylation?

1 reference

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Evolution of distinct EGF domains with specific functions

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Development of a carbon dioxide-capture assay in microtiter plate for aspartyl-beta-hydroxylase

1 reference

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Modifications of vectors pEF-BOS, pcDNA1 and pcDNA3 result in improved convenience and expression

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Identifiers

10.1016/S0076-6879(07)35004-0

1 reference

Europe PubMed Central

https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:17998049%20AND%20SRC:MED&resulttype=core&format=json

10 January 2020

1 reference

Europe PubMed Central

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10 January 2020

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